Size Limit in protein NMR – MSc Project

Pushing the Upper Size Limit in Protein NMR
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By Robert Griffin 

Question:

One of the major limitations of NMR as a technique has been the size of macromolecule that can be studied. There have been a number of methods proposed over the last few years to increase this size limit and these should be reviewed in this project. These include perdeuteration, residual dipolar coupling and TROSY. This project could also look at the increase in the size of NMR deposited structures in the PDB with time. Identify advances in the past that have been responsible for the increase in the upper size limit of the technique.

Introduction

This web review is a project for the ‘Trends in Structural Molecular Biology’ course at Birkbeck College. It can be navigated from this Home Page, sequentially using the links at the bottom right of each page or alternatively using the links on the mind map. To return to this Home Page at any time use the Home Page Link at the bottom left of each page.

Why is there a size limit in Protein NMR?

NMR Structures over Time

How have techniques been improved to push forward the size barrier?

Instrumentation

Labeling

Experimental Methods

Other Strategies

Case Studies

Gro-EL / Gro-ES

The Proteasome

Malate Synthase

Conclusions

Links and Acknowledgements

References


Why is there a size limit in Protein NMR?